Cloned (Comment) | Organism |
---|---|
baculovirus expression | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
DELTA2.5OGT | Baculovirus-produced recombinant, is partially active toward the OID protein substrate, but is fully active toward the CKII peptide substrate | Rattus norvegicus |
DELTA5.5OGT | Baculovirus-produced recombinant | Rattus norvegicus |
full-length OGT | Baculovirus-produced recombinant | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the isolated tetratricopeptide repeat domain of OGT competitively inhibits glycosylation of the OID protein, but does not inhibit glycosylation of small peptides, providing kinetic evidence for the role of the tetratricopeptide repeat domain as a protein substrate docking site | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00335 | - |
OIP106 protein | apparent Km of OGT for the OID of OIP106 protein | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Rattus norvegicus | enzyme catalyzes the abundant and dynamic posttranslational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
casein kinase II peptide + UDP-GlcNAc | - |
Rattus norvegicus | ? + UDP | - |
? | |
additional information | enzyme catalyzes the abundant and dynamic posttranslational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) | Rattus norvegicus | ? | - |
? | |
additional information | DELTA859 is not able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 | Rattus norvegicus | ? | - |
? | |
additional information | OGT-interacting proteins interact strongly with the tetratricopeptide repeat (TPR) domain of OGT, they are modified by O-GlcNAc and are excellent substrates of OGT | Rattus norvegicus | ? | - |
? | |
nucleoporin p62 + UDP-GlcNAc | high affinity substrate | Rattus norvegicus | ? + UDP | - |
? | |
OIP106 protein + UDP-GlcNAc | N-terminal deletions of OIP106 are generated as S-tagged constructs: DELTAnCC, DELTA491, DELTA639, DELTA859 | Rattus norvegicus | O-GlcNAc-OIP106 protein + UDP | - |
? | |
UDP-GlcNAc + DELTA639 protein | N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 | Rattus norvegicus | UDP + N-acetyl-D-glucosaminyl-[DELTA639 protein] | - |
? | |
UDP-GlcNAc + DELTAnCC protein | N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 | Rattus norvegicus | UDP + N-acetyl-D-glucosaminyl-[DELTAnCC protein] | - |
? | |
UDP-GlcNAc DELTA491 protein | N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 | Rattus norvegicus | UDP + N-acetyl-D-glucosaminyl-[DELTA491 protein] | - |
? |
Synonyms | Comment | Organism |
---|---|---|
O-GlcNAc transferase | - |
Rattus norvegicus |
OGT | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Rattus norvegicus |